PABA_BACSU
ID PABA_BACSU Reviewed; 194 AA.
AC P28819;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aminodeoxychorismate/anthranilate synthase component 2;
DE Short=ADC synthase;
DE Short=ADCS;
DE EC=2.6.1.85 {ECO:0000305|PubMed:2123867};
DE EC=4.1.3.27;
DE AltName: Full=4-amino-4-deoxychorismate synthase component 2;
DE AltName: Full=Aminodeoxychorismate synthase, glutamine amidotransferase component;
GN Name=pabA {ECO:0000303|PubMed:9384377};
GN Synonyms=trpG {ECO:0000303|PubMed:2123867}; OrderedLocusNames=BSU00750;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ASB342;
RX PubMed=2123867; DOI=10.1128/jb.172.12.7211-7226.1990;
RA Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.;
RT "An apparent Bacillus subtilis folic acid biosynthetic operon containing
RT pab, an amphibolic trpG gene, a third gene required for synthesis of para-
RT aminobenzoic acid, and the dihydropteroate synthase gene.";
RL J. Bacteriol. 172:7211-7226(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Part of a heterodimeric complex that catalyzes the two-step
CC biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-
CC aminobenzoate (PABA) and tetrahydrofolate. In the first step, a
CC glutamine amidotransferase (PabA) generates ammonia as a substrate
CC that, along with chorismate, is used in the second step, catalyzed by
CC aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts
CC glutamine into glutamate only in the presence of stoichiometric amounts
CC of PabB. Also involved in the biosynthesis of anthranilate (By
CC similarity). Complements a glutamine amidotransferase-negative mutant
CC (PubMed:2123867). {ECO:0000250|UniProtKB:P00903,
CC ECO:0000269|PubMed:2123867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-
CC glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85;
CC Evidence={ECO:0000305|PubMed:2123867};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC -!- SUBUNIT: Monomer. Heterodimer consisting of two non-identical subunits:
CC a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate
CC synthase subunit (PabB) (By similarity).
CC {ECO:0000250|UniProtKB:P00903}.
CC -!- INDUCTION: Repressed by tryptophan. {ECO:0000305|PubMed:2123867}.
CC -!- DISRUPTION PHENOTYPE: Requires tryptophan and has a partial requirement
CC for p-aminobenzoic acid for growth. {ECO:0000269|PubMed:2123867}.
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DR EMBL; M34053; AAA22695.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05310.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11851.1; -; Genomic_DNA.
DR PIR; B37854; B37854.
DR RefSeq; NP_387956.1; NC_000964.3.
DR RefSeq; WP_003243797.1; NZ_JNCM01000028.1.
DR AlphaFoldDB; P28819; -.
DR SMR; P28819; -.
DR STRING; 224308.BSU00750; -.
DR MEROPS; C26.955; -.
DR PaxDb; P28819; -.
DR PRIDE; P28819; -.
DR EnsemblBacteria; CAB11851; CAB11851; BSU_00750.
DR GeneID; 936441; -.
DR KEGG; bsu:BSU00750; -.
DR PATRIC; fig|224308.179.peg.75; -.
DR eggNOG; COG0512; Bacteria.
DR InParanoid; P28819; -.
DR OMA; HQVVIYR; -.
DR PhylomeDB; P28819; -.
DR BioCyc; BSUB:BSU00750-MON; -.
DR BioCyc; MetaCyc:BSU00750-MON; -.
DR SABIO-RK; P28819; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IMP:UniProtKB.
DR GO; GO:0004049; F:anthranilate synthase activity; IMP:UniProtKB.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:UniProtKB.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Folate biosynthesis; Glutamine amidotransferase; Lyase; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT CHAIN 1..194
FT /note="Aminodeoxychorismate/anthranilate synthase component
FT 2"
FT /id="PRO_0000056848"
FT DOMAIN 1..194
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 194 AA; 21685 MW; 7167D43557DEB37A CRC64;
MILMIDNYDS FTYNLVQYLG ELGEELVVKR NDSITIDEIE ELSPDFLMIS PGPCSPDEAG
ISLEAIKHFA GKIPIFGVCL GHQSIAQVFG GDVVRAERLM HGKTSDIEHD GKTIFEGLKN
PLVATRYHSL IVKPETLPSC FTVTAQTKEG EIMAIRHNDL PIEGVQFHPE SIMTSFGKEM
LRNFIETYRK EVIA
